Linolenate 9R-lipoxygenase (EC 1.13.11.61, NspLOX, (9R)-LOX, linoleate 9R-dioxygenase) is an enzyme with systematic name alpha-linolenate:oxygen (9R)-oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
| Linolenate 9R-lipoxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.61 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- alpha-linolenate + O2 (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate
In cyanobacteria the enzyme is involved in oxylipin biosynthesis.
References
edit- ^ Jernerén F, Hoffmann I, Oliw EH (March 2010). "Linoleate 9R-dioxygenase and allene oxide synthase activities of Aspergillus terreus". Archives of Biochemistry and Biophysics. 495 (1): 67–73. doi:10.1016/j.abb.2009.12.022. PMID 20043865.
- ^ Andreou AZ, Vanko M, Bezakova L, Feussner I (June 2008). "Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms". Phytochemistry. 69 (9): 1832–7. doi:10.1016/j.phytochem.2008.03.002. PMID 18439634.
- ^ Lang I, Göbel C, Porzel A, Heilmann I, Feussner I (March 2008). "A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120" (PDF). The Biochemical Journal. 410 (2): 347–57. doi:10.1042/BJ20071277. PMID 18031288.
External links
edit- Linolenate+9R-lipoxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
